What question did this study set out to answer?

Purify and characterize the neutral metalloendopeptidase enkephalinase from human kidney tissue and determine its cleavage specificity toward biologically active peptides.

June 1, 1983Biochemistry

Human kidney "enkephalinase", a neutral metalloendopeptidase that cleaves active peptides

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Authors

JGJohn T. GaffordThe University of Texas Health Science Center at San Antonio RSRandal A. SkidgelUniversity of Pisa EEErvin G. ErdösGeneral / Preventive / Lipids

Discussion

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Implication

Biochemical study demonstrates broad peptide-cleaving activity of human kidney enkephalinase, indicating a key regulatory role in metabolizing bradykinin and angiotensin.

Key Points

Purify and characterize the neutral metalloendopeptidase enkephalinase from human kidney tissue and determine its cleavage specificity toward biologically active peptides.
Extracted converting enzyme and solubilized enkephalinase activity from human kidney membrane fractions using Triton X-100.
Purified the enzyme to homogeneity via ion-exchange chromatography, tracking cleavage of Leu5-enkephalin at the Gly3-Phe4 bond.
Characterized enzymatic activity, inhibitor profiles, and cleavage sites using synthetic peptide substrates, bradykinin, angiotensin I, and angiotensin II.
The major enkephalinase form was purified 1140-fold to homogeneity with a 14% yield and achieved a specific activity of 46 mumol min⁻¹ mg⁻¹ toward Leu5-enkephalin.
The enzyme acted as a neutral metalloendopeptidase that inactivated bradykinin by releasing its C-terminal dipeptide, showing higher relative activity toward larger substrates than converting enzyme.
The peptidase cleaved angiotensin I at Pro7-Phe8 without converting it to angiotensin II, and inactivated angiotensin II by cleaving the Tyr4-Ile5 bond.

Cite This Study

Gafford et al. (1983) studied this question.

synapsesocial.com/papers/6a733fc2a7d283abeec236ee https://doi.org/10.1021/bi00282a035

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June 1, 1983Biochemistry

Human kidney "enkephalinase", a neutral metalloendopeptidase that cleaves active peptides

View Full Paper

Ask AI

Bookmark

Authors

JGJohn T. GaffordThe University of Texas Health Science Center at San Antonio RSRandal A. SkidgelUniversity of Pisa EEErvin G. ErdösGeneral / Preventive / Lipids

Discussion

Member takes

Implication

Biochemical study demonstrates broad peptide-cleaving activity of human kidney enkephalinase, indicating a key regulatory role in metabolizing bradykinin and angiotensin.

Key Points

Purify and characterize the neutral metalloendopeptidase enkephalinase from human kidney tissue and determine its cleavage specificity toward biologically active peptides.
Extracted converting enzyme and solubilized enkephalinase activity from human kidney membrane fractions using Triton X-100.
Purified the enzyme to homogeneity via ion-exchange chromatography, tracking cleavage of Leu5-enkephalin at the Gly3-Phe4 bond.
Characterized enzymatic activity, inhibitor profiles, and cleavage sites using synthetic peptide substrates, bradykinin, angiotensin I, and angiotensin II.
The major enkephalinase form was purified 1140-fold to homogeneity with a 14% yield and achieved a specific activity of 46 mumol min⁻¹ mg⁻¹ toward Leu5-enkephalin.
The enzyme acted as a neutral metalloendopeptidase that inactivated bradykinin by releasing its C-terminal dipeptide, showing higher relative activity toward larger substrates than converting enzyme.
The peptidase cleaved angiotensin I at Pro7-Phe8 without converting it to angiotensin II, and inactivated angiotensin II by cleaving the Tyr4-Ile5 bond.

Cite This Study

Gafford et al. (1983) studied this question.

synapsesocial.com/papers/6a733fc2a7d283abeec236ee https://doi.org/10.1021/bi00282a035

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